Proteomic analysis of protein adsorption: Serum amyloid P adsorbs to materials and promotes leukocyte adhesion

Jin Ku Kim, Evan A. Scott, Donald L. Elbert*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

Serum and plasma protein adsorption on materials was analyzed using gel electrophoresis and ion trap mass spectrometry, Following incubation of polypropylene, polyethylene terephthalate (PET), or polydimethylsiloxane (PDMS) with 5% serum for longer than 4 h, we found unexpectedly high amounts of the pentraxin serum amyloid P. It was previously shown that serum amyloid P is constitutively expressed in humans, functions as an opsonin, and interacts with the Fcγ receptors on leukocytes. We demonstrate that serum amyloid P adsorbed to tissue culture polystyrene, PDMS, and PET promotes the adhesion of granulocytes and monocytes in the presence of calcium. The methods developed for these studies may be useful for the large-scale study of protein adsorption and do not rely on radiolabeling or the availability of antibodies.

Original languageEnglish (US)
Pages (from-to)199-209
Number of pages11
JournalJournal of Biomedical Materials Research - Part A
Volume75
Issue number1
DOIs
StatePublished - Oct 1 2005

Keywords

  • Leukocyte
  • Protein adsorption
  • Proteomics
  • Serum amyloid P

ASJC Scopus subject areas

  • Ceramics and Composites
  • Biomaterials
  • Biomedical Engineering
  • Metals and Alloys

Fingerprint Dive into the research topics of 'Proteomic analysis of protein adsorption: Serum amyloid P adsorbs to materials and promotes leukocyte adhesion'. Together they form a unique fingerprint.

Cite this